The StpA protein functions as a molecular adapter to mediate repression of the bgl operon by truncated H-NS in Escherichia coli.
The mechanism of repression of the beta-glucoside utilization (bgl) operon of Escherichia coli by a carboxy-terminally truncated derivative of the nucleoid-associated protein H-NS which is defective in DNA binding was investigated. The DNA-binding function of the H-NS-like protein StpA was found to be necessary for repression, which is consistent with a role for StpA as a DNA-binding adapter for mutant derivatives of H-NS.
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Department of Microbiology, Moyne Institute of Preventive Medicine, Trinity College, Dublin 2, Republic of Ireland. Andrew.Free@ed.ac.uk
Williams
R M
RM
Dorman
C J
CJ
D026905:Amino Acid Transport Systems; D001426:Bacterial Proteins / Q000096:biosynthesis; D002352:Carrier Proteins / Q000096:biosynthesis; D004268:DNA-Binding Proteins / Q000235:genetics*; D004794:Enzyme Repression; D004926:Escherichia coli / Q000235:genetics*; D029968:Escherichia coli Proteins; D015964:Gene Expression Regulation, Bacterial; D017930:Genes, Reporter; D005960:Glucosides / Q000378:metabolism*; D018832:Molecular Chaperones; D009154:Mutation; D009876:Operon; D010446:Peptide Fragments / Q000235:genetics; D017384:Sequence Deletion
D026905:Amino Acid Transport Systems; D001426:Bacterial Proteins; D002352:Carrier Proteins; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D005960:Glucosides; C031908:H-NS protein, bacteria; D018832:Molecular Chaperones; D010446:Peptide Fragments; C060774:ProU protein, Bacteria; C090104:StpA protein, E coli